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Home / Equine Research Bank / J Vet Intern Med / Fibrinogen heterogeneity in horses.
Journal of veterinary internal medicine2021; 35(2); 1131-1139; doi: 10.1111/jvim.16065

Fibrinogen heterogeneity in horses.

Abstract: Fibrinogen heterogeneity has been observed in humans and can influence fibrinogen measurements when using the modified Clauss assay. We hypothesized that fibrinogen heterogeneity also exists in horses. Objective: To determine whether fibrinogen heterogeneity exists in horses. Methods: Five clinically healthy horses from the university equine teaching herd. Methods: Presumed fibrinogen was purified from pooled citrated plasma and electrophoresis performed. The purified protein was subjected to Western blotting using sheep antiserum against human fibrinogen, and liquid chromatography-tandem mass spectrometry (LC-MS/MS). Results: Gel electrophoresis of nonreduced equine purified protein yielded 2 protein bands (approximately 377 and 318 kDa) that corresponded with the molecular weights of human high molecular weight fibrinogen and low molecular weight fibrinogen fractions, respectively. Electrophoretograms of reduced purified protein, Western blots, and LC-MS/MS supported that the purified nonreduced protein bands were fibrinogen. Conclusions: Fibrinogen heterogeneity exists in horses.
© 2021 The Authors. Journal of Veterinary Internal Medicine published by Wiley Periodicals LLC. on behalf of the American College of Veterinary Internal Medicine.
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Publication Date: 2021-02-19 PubMed ID: 33604912PubMed Central: PMC7995376DOI: 10.1111/jvim.16065Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The researchers in this study identified different forms or variants (heterogeneity) of the protein fibrinogen in horses, much like what has been observed in humans. Their findings could influence how fibrinogen levels are measured in horses.

Research Objective

The main aim of this research was to establish whether there are different forms of fibrinogen (a blood-clotting protein) in horses, in a similar fashion to humans. This phenomenon is referred to as fibrinogen heterogeneity. Finding out that fibrinogen has different forms in horses could possibly influence how its levels are measured.

Research Methodology

  • Five clinically healthy horses were sourced from the university’s equine teaching herd for blood withdrawal.
  • The blood drawn was treated with an anticoagulant (citrated), and fibrinogen was extracted from the plasma – the liquid part of the blood.
  • The purified fibrinogen was then subjected to gel electrophoresis – a lab technique used to separate proteins based on their size and charge. This was aimed at identifying potential fibrinogen variants.
  • The proteins identified through gel electrophoresis were further analysed using Western blotting – a technique to detect specific proteins – and using an antiserum against human fibrinogen.
  • They also used liquid chromatography-tandem mass spectrometry (LC-MS/MS) to perform a detailed analysis of the proteins.

Research Findings

  • When the researchers ran the purified protein samples through gel electrophoresis, they found two protein bands, which suggest two different forms or variants of fibrinogen in horses.
  • The weights of the protein bands corresponded with the weights of different forms of fibrinogen observed in humans — high molecular weight and low molecular weight fibrinogen.
  • The results from Western blot and LC-MS/MS analyses further confirmed that the protein bands were indeed variants of fibrinogen.

Conclusion

The researchers concluded that fibrinogen heterogeneity exists in horses, consistent with their research hypothesis. This adds to the understanding of the protein composition of horse blood and may influence how fibrinogen levels are measured.

Cite This Article

APA
Russell EB, Courtman NF, Santos LL, Tennent-Brown BS. (2021). Fibrinogen heterogeneity in horses. J Vet Intern Med, 35(2), 1131-1139. https://doi.org/10.1111/jvim.16065

Publication

Journal of veterinary internal medicine
ISSN: 1939-1676
NlmUniqueID: 8708660
Country: United States
Language: English
Volume: 35
Issue: 2
Pages: 1131-1139

Researcher Affiliations

Russell, Elise B
  • U-Vet Werribee Animal Hospital and Faculty of Veterinary and Agricultural Sciences, The University of Melbourne, Werribee, Victoria, Australia.
Courtman, Natalie F
  • U-Vet Werribee Animal Hospital and Faculty of Veterinary and Agricultural Sciences, The University of Melbourne, Werribee, Victoria, Australia.
Santos, Leilani L
  • U-Vet Werribee Animal Hospital and Faculty of Veterinary and Agricultural Sciences, The University of Melbourne, Werribee, Victoria, Australia.
Tennent-Brown, Brett S
  • U-Vet Werribee Animal Hospital and Faculty of Veterinary and Agricultural Sciences, The University of Melbourne, Werribee, Victoria, Australia.

MeSH Terms

  • Animals
  • Blotting, Western / veterinary
  • Chromatography, Liquid / veterinary
  • Fibrinogen
  • Horses
  • Sheep
  • Tandem Mass Spectrometry / veterinary

Grant Funding

  • University of Melbourne

Conflict of Interest Statement

Authors declare no conflict of interest.

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Citations

This article has been cited 1 times.
  1. Brown JE, Noormohammadi AH, Courtman NF. Immunoreactivity of canine, feline, and equine D-dimer with antibodies to human D-dimer. J Vet Intern Med 2024 Jan-Feb;38(1):187-196.
    doi: 10.1111/jvim.16888pubmed: 37950415google scholar: lookup
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